(data stored in SCRATCH zone)

SWISSPROT: A4F6F4_SACEN

ID   A4F6F4_SACEN            Unreviewed;       383 AA.
AC   A4F6F4;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   RecName: Full=Kynureninase {ECO:0000256|PIRNR:PIRNR038800};
DE            EC=3.7.1.3 {ECO:0000256|PIRNR:PIRNR038800};
GN   OrderedLocusNames=SACE_0279 {ECO:0000313|EMBL:CAL99628.1};
GN   ORFNames=A8924_0673 {ECO:0000313|EMBL:PFG93431.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99628.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99628.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99628.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93431.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93431.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-
CC       hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-
CC       hydroxyanthranilic acid (3-OHAA), respectively.
CC       {ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate +
CC         H(+) + L-alanine; Xref=Rhea:RHEA:25143, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:36559, ChEBI:CHEBI:57972,
CC         ChEBI:CHEBI:58125; EC=3.7.1.3;
CC         Evidence={ECO:0000256|PIRNR:PIRNR038800};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-kynurenine = anthranilate + H(+) + L-alanine;
CC         Xref=Rhea:RHEA:16813, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16567, ChEBI:CHEBI:57959, ChEBI:CHEBI:57972;
CC         EC=3.7.1.3; Evidence={ECO:0000256|PIRNR:PIRNR038800};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRNR:PIRNR038800};
CC   -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; L-
CC       alanine and anthranilate from L-kynurenine: step 1/1.
CC       {ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
CC       from L-kynurenine: step 2/3. {ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- SIMILARITY: Belongs to the kynureninase family.
CC       {ECO:0000256|PIRNR:PIRNR038800}.
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DR   EMBL; AM420293; CAL99628.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93431.1; -; Genomic_DNA.
DR   RefSeq; WP_011873004.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0279; -.
DR   EnsemblBacteria; CAL99628; CAL99628; SACE_0279.
DR   KEGG; sen:SACE_0279; -.
DR   eggNOG; COG3844; LUCA.
DR   HOGENOM; HOG000242437; -.
DR   KO; K01556; -.
DR   OrthoDB; 996960at2; -.
DR   BioCyc; SERY405948:SACE_RS01365-MONOMER; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0030429; F:kynureninase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006569; P:tryptophan catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR010111; Kynureninase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR14084; PTHR14084; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF038800; KYNU; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4F6F4.
DR   SWISS-2DPAGE; A4F6F4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728,
KW   ECO:0000313|Proteomes:UP000225825};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR038800,
KW   ECO:0000313|EMBL:CAL99628.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|PIRNR:PIRNR038800};
KW   Pyridoxal phosphate {ECO:0000256|PIRNR:PIRNR038800};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728}.
FT   DOMAIN      146    324       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
SQ   SEQUENCE   383 AA;  41364 MW;  C68FAF0FB311615B CRC64;
     MWTSTRPAAT ALDSADALAG LRVRYELPPG LIRLDGNSGG AAPSRTSARL RKFAEHRWME
     SCARRFAPDW ELEARTCAAK LARLIGAGEC ELTVAETTSV NLFKALVAAS RLRPEHSALA
     VGRDCFASDH YLARSAAAYT GTELLLFDDL AELPFDRVAV VALSHTDVRS GAVRDPVATT
     AALHEQGVLV LWELSESAGA LDVDLHAWNA DLAVGCGHRY LGGGPGAPAY WFVAERHQRE
     LGGRDRGCDG VLSQAASGFS GAPSTLALSE LRHGLSMLDG VSGAELEAKT GGLVSLFVDR
     LLRAPGVEIV PPRRGRRRGP QVSLRHPRAQ LVVAELFARG VVVDFVDPDL LRFSFAPSWL
     RYIDVWEAAE VVREVLEQLD RES
//

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